Fig. 2

Characterisation of oligomerisation of the TIR and death domains alone and full-length MyD88. a Increase of apparent brightnesses of diffusing species. Values of B parameters obtained for expressions at protein concentrations > 150 nM were averaged and normalised to the sfGFP monomer control. Clearly, the data show that only full-length MyD88 (red) is capable of forming large complexes, while the TIR domain (green) or the death domain (blue) form smaller oligomers. Inset: Expansion of the values obtained for TIR and death domains compared to sfGFP control. b FCS data in solution. Control based on GFP monomer (black). Correlation curves obtained for the TIR domain (green), death domain (blue) and full-length MyD88 (red). A clear shift in diffusion time can be seen between the full-length protein and the separate domains. FCS curves are representative traces from three repeated measurements. c Hydrodynamic radius normalised by the sfGFP control (black) calculated for the domains and full-length MyD88, indicating the increase of approximate physical size of the oligomeric species. Values are mean ± SD from three repeat measurements